Inhibition of thermolysin by bifunctional N-carboxyalkyl dipeptides.
暂无分享,去创建一个
[1] J. Delaisse,et al. A new synthetic inhibitor of mammalian tissue collagenase inhibits bone resorption in culture. , 1985, Biochemical and biophysical research communications.
[2] B. Matthews,et al. An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides. , 1984, Biochemistry.
[3] B. Matthews,et al. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases. , 1984, Biochemistry.
[4] B. Beaufrère,et al. Use of t-butyldimethylsilylation in the gas chromatographic/mass spectrometric analysis of physiologic compounds found in plasma using electron-impact ionization. , 1984, Analytical biochemistry.
[5] M. Orłowski,et al. Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. , 1984, Biochemistry.
[6] P. Bartlett,et al. Phosphonamidates as transition-state analogue inhibitors of thermolysin. , 1983, Biochemistry.
[7] J. Almenoff,et al. Membrane-bound kidney neutral metalloendopeptidase: interaction with synthetic substrates, natural peptides, and inhibitors. , 1983, Biochemistry.
[8] R. Galardy,et al. Inhibition of angiotensin converting enzyme by phosphoramidates and polyphosphates. , 1982, Biochemistry.
[9] B. Matthews,et al. Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis. , 1982, Biochemistry.
[10] A. Patchett,et al. Inhibition of thermolysin by N-carboxymethyl dipeptides. , 1981, Biochemical and biophysical research communications.
[11] C. A. Stone,et al. A new class of angiotensin-converting enzyme inhibitors , 1980, Nature.
[12] J. Powers,et al. Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography. , 1979, Biochemistry.
[13] J. Powers,et al. Inhibition of thermolysin and carboxypeptidase A by phosphoramidates. , 1979, Biochemistry.
[14] J. Powers,et al. Peptide hydroxamic acids as inhibitors of thermolysin. , 1978, Biochemistry.
[15] D W Cushman,et al. Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids. , 1977, Biochemistry.
[16] Kester Wr,et al. Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis. , 1977 .
[17] E. J. Miller,et al. Cleavage of Type II and III collagens with mammalian collagenase: site of cleavage and primary structure at the NH2-terminal portion of the smaller fragment released from both collagens. , 1976, Biochemistry.
[18] A. Kang,et al. Animal collagenases: specificity of action, and structures of the substrate cleavage site. , 1974, Biochemical and biophysical research communications.
[19] B. Matthews,et al. The structure of thermolysin: an electron density map at 2-3 A resolution. , 1972, Journal of molecular biology.
[20] E. Corey,et al. Protection of hydroxyl groups as tert-butyldimethylsilyl derivatives , 1972 .
[21] H. Tsuzuki,et al. Thermolysin: kinetic study with oligopeptides. , 1970, European journal of biochemistry.
[22] J. Feder,et al. Studies on the Bacillus subtilis neutral-protease- and Bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substrates. , 1970, Biochemistry.
[23] A. Berger,et al. On the size of the active site in proteases. I. Papain. , 1967, Biochemical and biophysical research communications.
[24] G. N. Wilkinson. Statistical estimations in enzyme kinetics. , 1961, The Biochemical journal.
[25] B. Roques,et al. New carboxyalkyl inhibitors of brain enkephalinase: synthesis, biological activity, and analgesic properties. , 1983, Journal of medicinal chemistry.
[26] C. Tsai,et al. MECHANISM OF DECARBOXYLATION OF MONOETHYL OXALACETATE. , 1972 .
[27] S. Colowick,et al. Methods in Enzymology , Vol , 1966 .